메뉴 건너뛰기




Volumn 69, Issue , 2017, Pages 410-421

Effect of dietary fibre polysaccharides on structure and thermal properties of gluten proteins – A study on gluten dough with application of FT-Raman spectroscopy, TGA and DSC

Author keywords

DSC; Fibre polysaccharides; FT Raman spectroscopy; Gluten proteins; TGA

Indexed keywords

AGGREGATES; AMINO ACIDS; CELLULOSE; HYDROGEN BONDS; PROTEINS; RAMAN SPECTROSCOPY; SULFUR COMPOUNDS; THERMODYNAMIC PROPERTIES; THERMOGRAVIMETRIC ANALYSIS;

EID: 85015046843     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.03.012     Document Type: Article
Times cited : (151)

References (42)
  • 1
    • 0000115895 scopus 로고    scopus 로고
    • Antistaling additives, flour type and sourdough process effects on functionality of whet doughs
    • Armero, E., Collar, C., Antistaling additives, flour type and sourdough process effects on functionality of whet doughs. Journal of Food Science(61), 1996, 299–303.
    • (1996) Journal of Food Science , Issue.61 , pp. 299-303
    • Armero, E.1    Collar, C.2
  • 2
    • 32944474540 scopus 로고    scopus 로고
    • Fish gelatin: Structure, gelling properties and interactions with egg albumin proteins
    • Badii, F., Howell, N.K., Fish gelatin: Structure, gelling properties and interactions with egg albumin proteins. Food Hydrocolloids 20 (2007), 630–640.
    • (2007) Food Hydrocolloids , vol.20 , pp. 630-640
    • Badii, F.1    Howell, N.K.2
  • 3
    • 34548473820 scopus 로고    scopus 로고
    • Consumer liking of refined and whole wheat breads
    • Bakke, A., Vickers, Z., Consumer liking of refined and whole wheat breads. Journal of Food Science 72 (2007), S473–S480.
    • (2007) Journal of Food Science , vol.72 , pp. S473-S480
    • Bakke, A.1    Vickers, Z.2
  • 6
    • 84872413885 scopus 로고    scopus 로고
    • Bran-induced changes in water structure and gluten conformation in model gluten dough studied by Fourier transform infrared spectroscopy
    • Bock, J.E., Damodaran, S., Bran-induced changes in water structure and gluten conformation in model gluten dough studied by Fourier transform infrared spectroscopy. Food Hydrocolloids 31 (2013), 146–155.
    • (2013) Food Hydrocolloids , vol.31 , pp. 146-155
    • Bock, J.E.1    Damodaran, S.2
  • 7
    • 47349134111 scopus 로고    scopus 로고
    • Assessment of rheological profile of fibre-enriched bread doughs by response surface methodology
    • Collar, C., Santos, E., Rossell, C.M., Assessment of rheological profile of fibre-enriched bread doughs by response surface methodology. Journal of Food Engineering 78 (2007), 820–826.
    • (2007) Journal of Food Engineering , vol.78 , pp. 820-826
    • Collar, C.1    Santos, E.2    Rossell, C.M.3
  • 8
    • 84886087345 scopus 로고    scopus 로고
    • Interaction of modified celluloses and pectins with gluten proteins
    • Correa, M.J., Ferrer, E., Anon, M.C., Ferrero, C., Interaction of modified celluloses and pectins with gluten proteins. Food Hydrocolloids 35 (2014), 91–99.
    • (2014) Food Hydrocolloids , vol.35 , pp. 91-99
    • Correa, M.J.1    Ferrer, E.2    Anon, M.C.3    Ferrero, C.4
  • 9
    • 84922680055 scopus 로고    scopus 로고
    • Physical and sensory analysis of high fibre bread incorporated with jackfruit rind flour
    • Feili, R., Wahidu, Z.N., Wan Abdullah, T., Yang, A., Physical and sensory analysis of high fibre bread incorporated with jackfruit rind flour. Food Science and Technology 1 (2013), 30–36.
    • (2013) Food Science and Technology , vol.1 , pp. 30-36
    • Feili, R.1    Wahidu, Z.N.2    Wan Abdullah, T.3    Yang, A.4
  • 10
    • 79955668930 scopus 로고    scopus 로고
    • Structural changes in gluten protein structure after addition of emulsifier. A Raman spectroscopy study
    • Ferrer, E.G., Gomez, A.V., Anon, M.C., Puppo, M.C., Structural changes in gluten protein structure after addition of emulsifier. A Raman spectroscopy study. Spectrochimica Acta A 79 (2011), 278–281.
    • (2011) Spectrochimica Acta A , vol.79 , pp. 278-281
    • Ferrer, E.G.1    Gomez, A.V.2    Anon, M.C.3    Puppo, M.C.4
  • 12
    • 33750497845 scopus 로고    scopus 로고
    • Xanthophyll-induced aggregation of LHCII as a switch between light-harvesting and energy dissipation systems
    • Gruszecki, W.I., Grudziński, W., Gospodarek, M., Patyra, M., Maksymiec, W., Xanthophyll-induced aggregation of LHCII as a switch between light-harvesting and energy dissipation systems. Biochimica et Biophysica Acta 1757 (2006), 1504–1511.
    • (2006) Biochimica et Biophysica Acta , vol.1757 , pp. 1504-1511
    • Gruszecki, W.I.1    Grudziński, W.2    Gospodarek, M.3    Patyra, M.4    Maksymiec, W.5
  • 14
    • 0020489572 scopus 로고
    • Raman spectroscopy of avidin: Secondary structure, disulphide conformation and the environment of tyrosine
    • Honzatko, R.B., Williams, R.W., Raman spectroscopy of avidin: Secondary structure, disulphide conformation and the environment of tyrosine. Biochemistry 21 (1982), 6201–6205.
    • (1982) Biochemistry , vol.21 , pp. 6201-6205
    • Honzatko, R.B.1    Williams, R.W.2
  • 15
    • 61749086594 scopus 로고    scopus 로고
    • FTIR spectroscopic studies on aggregation process of the β-amyloid 11-28 fragment and its variants
    • Juszczyk, P., Kołodziejczyk, A., Grzonka, Z., FTIR spectroscopic studies on aggregation process of the β-amyloid 11-28 fragment and its variants. Journal of Peptide Science 15 (2009), 23–29.
    • (2009) Journal of Peptide Science , vol.15 , pp. 23-29
    • Juszczyk, P.1    Kołodziejczyk, A.2    Grzonka, Z.3
  • 16
    • 84870567888 scopus 로고    scopus 로고
    • Effects of gliadin addition on the rheological, microscopic and thermal characteristics of wheat gluten
    • Khatkar, B.S., Barak, S., Mudgil, D., Effects of gliadin addition on the rheological, microscopic and thermal characteristics of wheat gluten. International Journal of Biological Macromolecules 53 (2013), 38–41.
    • (2013) International Journal of Biological Macromolecules , vol.53 , pp. 38-41
    • Khatkar, B.S.1    Barak, S.2    Mudgil, D.3
  • 18
    • 0036187342 scopus 로고    scopus 로고
    • Effect of intermolecular disulphide bond on the conformation and stability of glial cell line-derived neurotrophic factor
    • Li, T., Yamane, H., Arakawa, T., Narhi, L.O., Philo, J., Effect of intermolecular disulphide bond on the conformation and stability of glial cell line-derived neurotrophic factor. Protein Engineering 15 (2002), 59–64.
    • (2002) Protein Engineering , vol.15 , pp. 59-64
    • Li, T.1    Yamane, H.2    Arakawa, T.3    Narhi, L.O.4    Philo, J.5
  • 20
    • 0035114404 scopus 로고    scopus 로고
    • Evolution of wheat gliadins conformation during film formation: A fourier transform infrared study
    • Mangavel, C., Barbot, J., Popineau, Y., Gueguen, J., Evolution of wheat gliadins conformation during film formation: A fourier transform infrared study. Journal of Agricultural Food Chemistry 49 (2001), 867–872.
    • (2001) Journal of Agricultural Food Chemistry , vol.49 , pp. 867-872
    • Mangavel, C.1    Barbot, J.2    Popineau, Y.3    Gueguen, J.4
  • 21
    • 0037433629 scopus 로고    scopus 로고
    • Observing the water molecule in macromolecules and aqueous media using infrared spectrometry
    • Marechal, Y., Observing the water molecule in macromolecules and aqueous media using infrared spectrometry. Journal of Molecular Structure 648 (2003), 27–47.
    • (2003) Journal of Molecular Structure , vol.648 , pp. 27-47
    • Marechal, Y.1
  • 22
    • 0037409125 scopus 로고    scopus 로고
    • Raman spectroscopic study of globulin from Phaseolus angularis (red bean)
    • Meng, G., Ma, C.-Y., Phillips, D.L., Raman spectroscopic study of globulin from Phaseolus angularis (red bean). Food Chemistry 81 (2003), 411–420.
    • (2003) Food Chemistry , vol.81 , pp. 411-420
    • Meng, G.1    Ma, C.-Y.2    Phillips, D.L.3
  • 24
    • 85027958044 scopus 로고    scopus 로고
    • Influence of dietary fibre on gluten proteins structure – a study on model flour with application of FT-Raman spectroscopy
    • Nawrocka, A., Szymańska-Chargot, M., Miś, A., Ptaszyńska, A.A., Kowalski, R., Waśko, P., et al. Influence of dietary fibre on gluten proteins structure – a study on model flour with application of FT-Raman spectroscopy. Journal of Raman Spectroscopy 46 (2015), 309–316.
    • (2015) Journal of Raman Spectroscopy , vol.46 , pp. 309-316
    • Nawrocka, A.1    Szymańska-Chargot, M.2    Miś, A.3    Ptaszyńska, A.A.4    Kowalski, R.5    Waśko, P.6
  • 26
    • 84961839565 scopus 로고    scopus 로고
    • Dietary fibre-induced changes in the structure and thermal properties of gluten proteins studied by Fourier transform-Raman spectroscopy and thermogravimetry
    • Nawrocka, A., Szymańska-Chargot, M., Miś, A., Wilczewska, A.Z., Markiewicz, K.H., Dietary fibre-induced changes in the structure and thermal properties of gluten proteins studied by Fourier transform-Raman spectroscopy and thermogravimetry. Journal of Agricultural and Food Chemistry 64 (2016), 2094–2104.
    • (2016) Journal of Agricultural and Food Chemistry , vol.64 , pp. 2094-2104
    • Nawrocka, A.1    Szymańska-Chargot, M.2    Miś, A.3    Wilczewska, A.Z.4    Markiewicz, K.H.5
  • 27
    • 84957430495 scopus 로고    scopus 로고
    • Characteristics of relationships between structure of gluten proteins and dough rheology – influence of dietary fibres studied by FT-Raman spectroscopy
    • Nawrocka, A., Miś, A., Szymańska-Chargot, M., Characteristics of relationships between structure of gluten proteins and dough rheology – influence of dietary fibres studied by FT-Raman spectroscopy. Food Biophysics 11 (2016), 81–90.
    • (2016) Food Biophysics , vol.11 , pp. 81-90
    • Nawrocka, A.1    Miś, A.2    Szymańska-Chargot, M.3
  • 28
    • 0024506309 scopus 로고
    • Structure-function relationships in the inorganic salt-induced precipitation of α-chymotrypsin
    • Przybycien, T.M., Bailey, J.E., Structure-function relationships in the inorganic salt-induced precipitation of α-chymotrypsin. Biochimica et Biophysica Acta 995 (1989), 231–245.
    • (1989) Biochimica et Biophysica Acta , vol.995 , pp. 231-245
    • Przybycien, T.M.1    Bailey, J.E.2
  • 29
    • 0026020904 scopus 로고
    • Secondary structure perturbations in salt-induced proteins precipitates
    • Przybycien, T.M., Bailey, J.E., Secondary structure perturbations in salt-induced proteins precipitates. Biochimica et Biophysica Acta 1076 (1991), 103–111.
    • (1991) Biochimica et Biophysica Acta , vol.1076 , pp. 103-111
    • Przybycien, T.M.1    Bailey, J.E.2
  • 31
    • 0038538239 scopus 로고    scopus 로고
    • Sulfhydryl-disulphide changes in storage proteins of developing wheat grain: Influence on the SDS-unextractable glutenin polymer formation
    • Rhazi, L., Cazalis, R., Aussenac, T., Sulfhydryl-disulphide changes in storage proteins of developing wheat grain: Influence on the SDS-unextractable glutenin polymer formation. Journal of Cereal Science 2003:38 (2003), 3–13.
    • (2003) Journal of Cereal Science , vol.2003 , Issue.38 , pp. 3-13
    • Rhazi, L.1    Cazalis, R.2    Aussenac, T.3
  • 32
    • 14644425920 scopus 로고    scopus 로고
    • ATR-FT/IR study on interactions between gliadins and dextrin and their effects on protein secondary structure
    • Secundo, F., Guerrieri, N., ATR-FT/IR study on interactions between gliadins and dextrin and their effects on protein secondary structure. Journal of Agricultural and Food Chemistry 53 (2005), 1757–1764.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 1757-1764
    • Secundo, F.1    Guerrieri, N.2
  • 33
    • 0016824687 scopus 로고
    • -1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds
    • -1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds. Biochemistry 14 (1975), 4870–4876.
    • (1975) Biochemistry , vol.14 , pp. 4870-4876
    • Siamwiza, M.N.1    Lord, R.C.2    Chen, M.C.3
  • 34
    • 58149154652 scopus 로고    scopus 로고
    • Effect of barley b-glucan molecular size and level on wheat dough rheological properties
    • Skendi, A., Papageorgiou, M., Biliaderis, C.G., Effect of barley b-glucan molecular size and level on wheat dough rheological properties. Journal of Food Engineering 91 (2009), 594–601.
    • (2009) Journal of Food Engineering , vol.91 , pp. 594-601
    • Skendi, A.1    Papageorgiou, M.2    Biliaderis, C.G.3
  • 36
    • 42649121376 scopus 로고    scopus 로고
    • Glass transition temperature and thermal decomposition of cellulose powder
    • Szcześniak, L., Rachocki, A., Tritt-Goc, J., Glass transition temperature and thermal decomposition of cellulose powder. Cellulose 15 (2008), 445–451.
    • (2008) Cellulose , vol.15 , pp. 445-451
    • Szcześniak, L.1    Rachocki, A.2    Tritt-Goc, J.3
  • 37
    • 84886310365 scopus 로고    scopus 로고
    • Effect of frozen storage on the conformational, thermal and microscopic properties of gluten: Comparative studies on gluten-, glutenin- and gliadin-rich fractions
    • Wang, P., Xu, L., Nikoo, M., Ocen, D., Wu, F., Yang, N., et al. Effect of frozen storage on the conformational, thermal and microscopic properties of gluten: Comparative studies on gluten-, glutenin- and gliadin-rich fractions. Food Hydrocolloids 35 (2014), 238–246.
    • (2014) Food Hydrocolloids , vol.35 , pp. 238-246
    • Wang, P.1    Xu, L.2    Nikoo, M.3    Ocen, D.4    Wu, F.5    Yang, N.6
  • 38
    • 0029952769 scopus 로고    scopus 로고
    • Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of ω-gliadins
    • Wellner, N., Belton, P.S., Tatham, A.S., Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of ω-gliadins. Biochemical Journal 319 (1996), 741–747.
    • (1996) Biochemical Journal , vol.319 , pp. 741-747
    • Wellner, N.1    Belton, P.S.2    Tatham, A.S.3
  • 39
    • 14044265534 scopus 로고    scopus 로고
    • Changes in protein secondary structure during gluten deformation studied by dynamic Fourier transform infrared spectroscopy
    • Wellner, R., Mills, E.N.C., Brownsey, G., Wilson, R.H., Brown, N., Freeman, J., et al. Changes in protein secondary structure during gluten deformation studied by dynamic Fourier transform infrared spectroscopy. Biomacromolecules 6 (2005), 255–261.
    • (2005) Biomacromolecules , vol.6 , pp. 255-261
    • Wellner, R.1    Mills, E.N.C.2    Brownsey, G.3    Wilson, R.H.4    Brown, N.5    Freeman, J.6
  • 40
    • 33748885488 scopus 로고    scopus 로고
    • Chemistry of gluten proteins
    • Wieser, H., Chemistry of gluten proteins. Food Microbiology 24 (2007), 115–119.
    • (2007) Food Microbiology , vol.24 , pp. 115-119
    • Wieser, H.1
  • 41
    • 84983627853 scopus 로고    scopus 로고
    • Effect of hydroxypropylmethylcellulose on transition of water status and physicochemical properties of wheat gluten upon frozen storage
    • Xuan, Y.-F., Zhang, Y., Zhao, Y.Y., Zheng, Z., Jiang, S.-T., Zong, X.-Y., Effect of hydroxypropylmethylcellulose on transition of water status and physicochemical properties of wheat gluten upon frozen storage. Food Hydrocolloids 63 (2017), 35–42.
    • (2017) Food Hydrocolloids , vol.63 , pp. 35-42
    • Xuan, Y.-F.1    Zhang, Y.2    Zhao, Y.Y.3    Zheng, Z.4    Jiang, S.-T.5    Zong, X.-Y.6
  • 42
    • 84881523244 scopus 로고    scopus 로고
    • Konjac glucomannan-induced changes in thiol-disulphide exchange and gluten conformation upon dough mixing
    • Zhou, Y., Zhao, D., Foster, T.J., Liu, Y., Wang, Y., Nirasawa, S., et al. Konjac glucomannan-induced changes in thiol-disulphide exchange and gluten conformation upon dough mixing. Food Chemistry 143 (2014), 163–169.
    • (2014) Food Chemistry , vol.143 , pp. 163-169
    • Zhou, Y.1    Zhao, D.2    Foster, T.J.3    Liu, Y.4    Wang, Y.5    Nirasawa, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.